eF-site ID 5l9e-C
PDB Code 5l9e
Chain C

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Title CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER
Classification Lyase/Inhibitor
Compound Carbonic anhydrase 2
Source (CAH2_HUMAN)
Sequence C:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
Description


Functional site
1) chain C
residue 26
type
sequence E
description binding site for residue ZN A 308
source : AC3
2) chain C
residue 171
type
sequence K
description binding site for residue ZN A 316
source : AD2
3) chain C
residue 233
type
sequence E
description binding site for residue ZN A 316
source : AD2
4) chain C
residue 233
type
sequence E
description binding site for residue ZN A 316
source : AD2
5) chain C
residue 94
type
sequence H
description binding site for residue ZN C 301
source : AD9
6) chain C
residue 96
type
sequence H
description binding site for residue ZN C 301
source : AD9
7) chain C
residue 119
type
sequence H
description binding site for residue ZN C 301
source : AD9
8) chain C
residue 4
type
sequence H
description binding site for residue ZN C 307
source : AE1
9) chain C
residue 64
type
sequence H
description binding site for residue ZN C 307
source : AE1
10) chain C
residue 17
type
sequence H
description binding site for residue ZN C 308
source : AE2
11) chain C
residue 174
type
sequence D
description binding site for residue ZN C 309
source : AE3
12) chain C
residue 34
type
sequence D
description binding site for residue ZN C 310
source : AE4
13) chain C
residue 36
type
sequence H
description binding site for residue ZN C 310
source : AE4
14) chain C
residue 62
type
sequence N
description binding site for residue GOL C 311
source : AE5
15) chain C
residue 67
type
sequence N
description binding site for residue GOL C 311
source : AE5
16) chain C
residue 94
type
sequence H
description binding site for residue GOL C 311
source : AE5
17) chain C
residue 199
type
sequence T
description binding site for residue GOL C 311
source : AE5
18) chain C
residue 36
type
sequence H
description binding site for residue ZN C 312
source : AE6
19) chain C
residue 92
type
sequence Q
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
20) chain C
residue 94
type
sequence H
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
21) chain C
residue 96
type
sequence H
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
22) chain C
residue 119
type
sequence H
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
23) chain C
residue 130
type
sequence F
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
24) chain C
residue 197
type
sequence L
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
25) chain C
residue 198
type
sequence T
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
26) chain C
residue 199
type
sequence T
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
27) chain C
residue 208
type
sequence W
description binding site for residues 6H0 C 302 and QUJ C 303
source : AG6
28) chain C
residue 4
type
sequence H
description binding site for residues QUJ C 303 and QVE C 304
source : AG7
29) chain C
residue 169
type
sequence K
description binding site for residues QUJ C 303 and QVE C 304
source : AG7
30) chain C
residue 4
type
sequence H
description binding site for residues QVE C 304 and QUJ C 305
source : AG8
31) chain C
residue 19
type
sequence D
description binding site for residues QVE C 304 and QUJ C 305
source : AG8
32) chain C
residue 20
type
sequence F
description binding site for residues QVE C 304 and QUJ C 305
source : AG8
33) chain C
residue 169
type
sequence K
description binding site for residues QVE C 304 and QUJ C 305
source : AG8
34) chain C
residue 4
type
sequence H
description binding site for residues QUJ C 305 and QVE C 306
source : AG9
35) chain C
residue 5
type
sequence W
description binding site for residues QUJ C 305 and QVE C 306
source : AG9
36) chain C
residue 19
type
sequence D
description binding site for residues QUJ C 305 and QVE C 306
source : AG9
37) chain C
residue 20
type
sequence F
description binding site for residues QUJ C 305 and QVE C 306
source : AG9
38) chain C
residue 64
type
sequence H
description binding site for residues QUJ C 305 and QVE C 306
source : AG9
39) chain C
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA3
40) chain C
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA3
41) chain C
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA3
42) chain C
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA3
43) chain C
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA3
44) chain C
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA3
45) chain C
residue 64
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI1
46) chain C
residue 92
type SITE
sequence Q
description Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI7
47) chain C
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
48) chain C
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
49) chain C
residue 94
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
source Swiss-Prot : SWS_FT_FI2
50) chain C
residue 96
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
source Swiss-Prot : SWS_FT_FI3
51) chain C
residue 119
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
source Swiss-Prot : SWS_FT_FI3
52) chain C
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
53) chain C
residue 7
type SITE
sequence Y
description Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI5
54) chain C
residue 62
type SITE
sequence N
description Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI6
55) chain C
residue 67
type SITE
sequence N
description Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI6

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